Protein refolding assisted by self-assembled nanogels as novel artificial molecular chaperone

FEBS Lett. 2003 Oct 23;553(3):271-6. doi: 10.1016/s0014-5793(03)01028-7.


Molecular chaperone-like activity for protein refolding was investigated using nanogels of self-assembly of cholesterol-bearing pullulan. Nanogels effectively prevented protein aggregation (i.e. carbonic anhydrase and citrate synthase) during protein refolding from GdmCl denaturation. Enzyme activity recovered in high yields upon dissociation of the gel structure in which the proteins were trapped, by the addition of cyclodextrins. The nanogels assisted protein refolding in a manner similar to the mechanism of molecular chaperones, namely by catching and releasing proteins. The nanogels acted as a host for the trapping of refolded intermediate proteins. Cyclodextrin is an effector molecule that controls the binding ability of these host nanogels to proteins. The present nanogel system was also effective at the renaturation of inclusion body of a recombinant protein of the serine protease family.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carbonic Anhydrases / chemistry*
  • Carbonic Anhydrases / metabolism
  • Cattle
  • Citrate (si)-Synthase / chemistry*
  • Citrate (si)-Synthase / metabolism
  • Cyclodextrins / chemistry
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics
  • Glucans / chemistry
  • Guanidine / chemistry
  • Hydrogels / chemistry*
  • Inclusion Bodies / chemistry
  • Inclusion Bodies / genetics
  • Kinetics
  • Molecular Chaperones / chemistry*
  • Protein Denaturation
  • Protein Folding
  • Protein Renaturation*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Swine


  • Cyclodextrins
  • Escherichia coli Proteins
  • Glucans
  • Hydrogels
  • Molecular Chaperones
  • Recombinant Proteins
  • pullulan
  • Citrate (si)-Synthase
  • Carbonic Anhydrases
  • Guanidine